Molecular Playground/Chymotrypsin

One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

Chymotrypsin (Alpha-Chymotrypsin Dimer ) is a proteolytic enzyme which cleaves peptide bonds. The enzyme shows selectively to peptides with aromatic sidechains on the carboxyl side of the peptide bond. This is due to a “hydrophobic pocket” near the active site of the enzyme. The protein also contains a large number of cationic residues.

In this depiction of the monomer Cationic Residues, the cationic amino acid residues on the protein (blue) can interact with anionic, functionalized nanoparticles. After the nanoparticle-protein complex is formed, chymotrypsin then displays a preference for cationic substrates due to interaction with the anionic nanoparticle. The active site of chymotrypsin is shown in red.



Molecular Playground banner: Chymotrypsin is a digestive enzyme that breaks down proteins